Proteome-wide analysis of lysine acetylation in adult Schistosoma japonicum worm

文献类型： 外文期刊

第一作者： Hong, Yang

作者： Hong, Yang;Cao, Xiaodan;Han, Qian;Yuan, Chunxiu;Zhu, Chuangang;Lu, Ke;Li, Hao;Fu, Zhiqiang;Lin, Jiaojiao;Zhang, Min;Han, Yanhui;Lin, Jiaojiao;Lin, Tao

作者机构：

关键词： Schistosoma japonicum;Posttranslational modifications;Lysine acetylation (LysAc);Acetylome;Adult worm

期刊名称：JOURNAL OF PROTEOMICS （ 影响因子：4.044； 五年影响因子：4.02 ）

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年卷期：

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收录情况： SCI

摘要： Lysine acetylation, a ubiquitous and conserved posttranslational modification, has recently been shown to participate in many diverse non-chromatin-associated biological processes in prokaryotes and eukaryotes. However, the full extent and functional significance of acetylation in Schistosoma japonicum is still unknown. To investigate the nature, extent, and biological functions of lysine acetylation in schistosomes, immunoaffinity-based acetyl lysine peptide enrichment, integrated with mass spectrometry, was used to comprehensively characterize the lysine-acetylated proteins in this parasite. In total, 1109 acetylated proteins and 2393 acetylation sites in S. japonicum were identified, representing the largest acetylome yet reported in a parasite. In a bioinformatic analysis showed that these acetylated proteins were mainly enriched in the biological process categories of metabolism, gene expression, translation, and transport. The classification according to molecular function revealed that the largest class involved the catalytic activity of different enzymes, including oxidoreductase, transferase, and pyrophosphatase activities. Most of the acetylated proteins in the cellular component category occurred in the cytoplasm, membrane, cytoskeleton, and nucleus. These data demonstrate the generality of lysine acetylation and provide the first global survey of acetylation in schistosomes. Our findings are an exciting starting point for the further exploration of the functions of acetylation in the biology of this parasite.

分类号： Q51

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